Structural highlights
Function
KMT_SULIR Catalyzes the methylation of lysine residues in target proteins, using S-adenosyl-L-methionine (SAM) as the methyl donor. Exhibits broad substrate specificity, being able to methylate the crenarchaeal chromatin protein Cren7 primarily at 'Lys-11', 'Lys-16' and 'Lys-31', as well as a number of recombinant Sulfolobus proteins in vitro. Methylates lysine residues in a rather sequence-independent manner.[1]
References
- ↑ Chu Y, Zhang Z, Wang Q, Luo Y, Huang L. Identification and characterization of a highly conserved crenarchaeal protein lysine methyltransferase with broad substrate specificity. J Bacteriol. 2012 Dec;194(24):6917-26. doi: 10.1128/JB.01535-12. Epub 2012 Oct, 19. PMID:23086207 doi:http://dx.doi.org/10.1128/JB.01535-12
